title: A comparative study of glycoproteomes in androgen-sensitive and -independent prostate cancer cell lines.
abstract: Prostate cancer is one of the most common malignancies in men and is predicted to be the second leading cause of cancer-related deaths. After 6-18 months, hormone ablation treatment results in androgen-independent growth of cancer cells, metastasis and progression. The mechanism of androgen-independent growth of prostatic carcinoma cells is still unknown. Identification of factors that facilitate the transition from androgen-dependent to independent states is crucial in designing future diagnostics and medication strategies. To understand the biochemical meaning of hormone dependency deprivation, glycoproteins enriched profiles were compared between DU145 (hormone non-responding) and LNCaP (hormone responding) prostate cancer cells. These results allow for anticipation on the important role of glycosylation in malignant transformation. Both Tn antigen and complex antennary N-oligosaccharides were recognized. Their occurrence might be involved in the development and progression of tumor, and failure of hormone ablation therapy. Among identified proteins in androgen-sensitive cells nucleolin (P19338) was found that is widely described as apoptosis inhibitor, and also transporter of molecules from the membrane to the cytoplasm or nucleus. In addition, 14-3-3 protein family (P27348, P31946, P61981, P63104, P62258, Q04917, and P31947) was investigated across available databases as it forms stable complexes with glycoproteins. Our studies indicate that isoforms: sigma and eta were found in androgen-dependent prostate cancer cells, while other isoforms were present in androgen non-responding cells. 14-3-3 binding partners are involved in cancer pathogenesis. These findings may contribute to a better understanding of prostate cancer tumorigenesis and to a more efficient prognosis and individual therapy in a future. However, it still remains to be revealed how important those changes are for androgen dependency loss in prostate cancer patients carried out on clinically relevant populations.
authors.affiliation: Department of Biochemistry and Neurobiology, AGH University of Science and Technology, Mickiewicza 30 Ave, 30-059, Krakow, Poland, drabik@agh.edu.pl.
authors.forename: Anna
authors.initials: A
authors.lastname: Drabik
authors.forename: Dorota
authors.initials: D
authors.lastname: Ciołczyk-Wierzbicka
authors.forename: Joanna
authors.initials: J
authors.lastname: Dulińska-Litewka
authors.forename: Anna
authors.initials: A
authors.lastname: Bodzoń-Kułakowska
authors.forename: Piotr
authors.initials: P
authors.lastname: Suder
authors.forename: Jerzy
authors.initials: J
authors.lastname: Silberring
authors.forename: Piotr
authors.initials: P
authors.lastname: Laidler
mesh_terms: D000728:Androgens / Q000502:physiology*; D015153:Blotting, Western; D045744:Cell Line, Tumor; D002471:Cell Transformation, Neoplastic; D002846:Chromatography, Affinity / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D006020:Glycopeptides / Q000378:metabolism*; D006801:Humans; D008297:Male; D009376:Neoplasms, Hormone-Dependent / Q000378:metabolism / Q000503:physiopathology*; D020543:Proteome; D053719:Tandem Mass Spectrometry
chemical_list: D000728:Androgens; D006020:Glycopeptides; D020543:Proteome